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Crystallization and preliminary X-ray analysis of TBP-interacting protein from the hyperthermophilic archaeonThermococcus kodakaraensisstrain KOD1
- Source :
- Acta Crystallographica Section D Biological Crystallography. 59:372-374
- Publication Year :
- 2003
- Publisher :
- International Union of Crystallography (IUCr), 2003.
-
Abstract
- The 26 kDa TBP (TATA-binding protein) interacting protein from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 (Tk-TIP26) is a possible transcriptional regulatory protein in Thermococcales. Here, the crystallization of both the native and selenomethionine-substituted proteins and data collection are described. The native crystals belong to the tetragonal space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = 73.83, c = 86.41 A, and diffract to 2.2 A using synchrotron radiation. MAD data was collected and a Bijvoet difference Patterson map showed strong peaks sufficient to determine the positions of the Se atoms.
- Subjects :
- biology
Archaeal Proteins
TBP interacting protein
General Medicine
Crystallography, X-Ray
TATA-Box Binding Protein
biology.organism_classification
Thermococcales
law.invention
Thermococcus
Tetragonal crystal system
Crystallography
Structural Biology
law
Escherichia coli
Crystallization
Selenomethionine
X ray analysis
Transcriptional Regulatory Protein
Synchrotrons
Subjects
Details
- ISSN :
- 09074449
- Volume :
- 59
- Database :
- OpenAIRE
- Journal :
- Acta Crystallographica Section D Biological Crystallography
- Accession number :
- edsair.doi.dedup.....3424f0648ef31427abfd777a1d240231
- Full Text :
- https://doi.org/10.1107/s090744490202142x